Compact fibril-like structure of amyloid β-peptide (1-42) monomers.
Compact fibril-like structure of amyloid β-peptide (1-42) monomers.
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淀粉样蛋白 β 肽 (1-42) 单体的紧凑原纤维样结构
DOI:
10.1039/d0cc06607a
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发表时间:
2021
影响因子:
4.9
通讯作者:
Nath S.
中科院分区:
文献类型:
--
作者:
Barz B;Buell A. K.;Nath S.
Amyloid β (Aβ) monomers are the smallest assembly units, and play an important role in most of the individual processes involved in amyloid fibril formation. An important question is whether the monomer can adopt transient fibril-like conformations in solution. Here we use enhanced sampling simulations to study the Aβ42 monomer structural flexibility. We show that the monomer frequently adopts conformations with the N-terminus region structured very similarly to the conformation it adopts inside the fibril. This intrinsic propensity of monomeric Aβ to adopt fibril-like conformations could explain the low free energy barrier for Aβ42 fibril elongation.
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DOI:
10.1016/j.bbrc.2011.06.133
发表时间:
2011-07-29
影响因子:
3.1
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Vivekanandan, Subramanian;Brender, Jeffrey R.;Lee, Shirley Y.;Ramamoorthy, Ayyalusamy
通讯作者:
Ramamoorthy, Ayyalusamy
影响因子:
2.9
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DOI:
--
发表时间:
2014
期刊:
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3.3
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